Abstract
A study has been made of the Tiselius electrophoresis of casein and casein fractions in veronal buffer containing urea. It was found that κ-casein migrates in the β-peak when urea level is increased. In the buffer containing urea level of 7.0M, both αs- and β-casein migrated in one peak but α-casein was resolved into 3 components. The most remarkable resolution could be obtained in the electrophoretic pattern of κ-casein preparation which migrated into at least six components.
The change in the electrophoretic pattern of whole casein solution when heated at temperature above 110°C for 30 minutes could be detected markedly using buffer containing 7 M urea. This indicates that the Tiselius electrophoresis using urea buffer is applicable for other investigation as rapid and simple method.
